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Activation of G protein-coupled receptors: beyond two-state models and tertiary conformational changes Park PS; Lodowski DT; Palczewski KAnnu Rev Pharmacol Toxicol 2008[]; 48 (ä): 107-41Transformation of G protein-coupled receptors (GPCRs) from a quiescent to an active state initiates signal transduction. All GPCRs share a common architecture comprising seven transmembrane-spanning alpha-helices, which accommodates signal propagation from a diverse repertoire of external stimuli across biological membranes to a heterotrimeric G protein. Signal propagation through the transmembrane helices likely involves mechanistic features common to all GPCRs. The structure of the light receptor rhodopsin may serve as a prototype for the transmembrane architecture of GPCRs. Early biochemical, biophysical, and pharmacological studies led to the conceptualization of receptor activation based on the context of two-state equilibrium models and conformational changes in protein structure. More recent studies indicate a need to move beyond these classical paradigms and to consider additional aspects of the molecular character of GPCRs, such as the oligomerization and dynamics of the receptor.|*Models, Molecular[MESH]|*Protein Structure, Tertiary[MESH]|Binding Sites[MESH]|Humans[MESH]|Ligands[MESH]|Molecular Structure[MESH]|Receptors, G-Protein-Coupled/*metabolism[MESH]|Rhodopsin/metabolism[MESH]|Signal Transduction[MESH] |
